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J. Biol. Chem., Vol. 276, Issue 16, 13025-13033, April 20, 2001
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From the Department of Chemistry & Biochemistry, University of
Oklahoma, Norman, Oklahoma 73019
The ferric siderophore transporters of the
Gram-negative bacterial outer membrane manifest a unique architecture:
Their N termini fold into a globular domain that lodges within, and
physically obstructs, a transmembrane porin
Exchangeability of N Termini in the Ligand-gated Porins of
Escherichia coli*
-barrel formed by
their C termini. We exchanged and deleted the N termini of two such
siderophore receptors, FepA and FhuA, which recognize and transport
ferric enterobactin and ferrichrome, respectively. The resultant
chimeric proteins and empty -barrels avidly bound appropriate
ligands, including iron complexes, protein toxins, and viruses. Thus,
the ability to recognize and discriminate these molecules fully
originates in the transmembrane -barrel domain. Both the hybrid and
the deletion proteins also transported the ferric siderophore that they
bound. The FepA constructs showed less transport activity than wild
type receptor protein, but the FhuA constructs functioned with turnover
numbers that were equivalent to wild type. The mutant proteins
displayed the full range of transport functionalities, despite their
aberrant or missing N termini, confirming (Braun, M., Killmann, H., and
Braun, V. (1999) Mol. Microbiol. 33, 1037-1049) that the
globular domain within the pore is dispensable to the siderophore internalization reaction, and when present, acts without specificity during solute uptake. These and other data suggest a
transport process in which siderophore receptors undergo multiple conformational states that ultimately expel the N terminus from the
channel concomitant with solute internalization.
*
This work was supported by National Science Foundation Grant
MCB9709418 and National Institutes of Health Grant GM53836.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Tel.: 405-325-4969;
Fax: 405-325-6111; E-mail: peklebba@ou.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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